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Relevant bibliographies by topics / Beta mercaptoethanol

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Journal articles

Academic literature on the topic 'Beta mercaptoethanol'

Author: Grafiati

Published: 7 June 2025

Last updated: 17 July 2025

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Journal articles on the topic "Beta mercaptoethanol"

1

Marra, E., S. Passarella, E. Casamassima, E. Perlino, S. Doonan, and E. Quagliariello. "Kinetic studies of the uptake of aspartate aminotransferase and malate dehydrogenase into mitochondria in vitro." Biochemical Journal 228, no. 2 (1985): 493–503. http://dx.doi.org/10.1042/bj2280493.

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Kinetic measurements of the uptake of native mitochondrial aspartate aminotransferase and malate dehydrogenase into mitochondria in vitro were carried out. The uptake of both the enzymes is essentially complete in 1 min and shows saturation characteristics. The rate of uptake of aspartate aminotransferase into mitochondria is decreased by malate dehydrogenase, and vice versa. The inhibition is exerted by isoenzyme remaining outside the mitochondria rather than by isoenzyme that has been imported. The thiol compound beta-mercaptoethanol decreases the rate of uptake of the tested enzymes; inhibi

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2

Click, Robert E. "Potential alteration of COVID-19 by beta-mercaptoethanol." Future Microbiology 15, no. 14 (2020): 1313–18. http://dx.doi.org/10.2217/fmb-2020-0142.

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3

Kim, Y. K., and A. S. Lee. "Transcriptional activation of the glucose-regulated protein genes and their heterologous fusion genes by beta-mercaptoethanol." Molecular and Cellular Biology 7, no. 8 (1987): 2974–76. http://dx.doi.org/10.1128/mcb.7.8.2974-2976.1987.

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The sulfhydryl-reducing agent beta-mercaptoethanol preferentially stimulates the synthesis of glucose-regulated proteins (GRPs) in mammalian cells. The rapid and large increase in GRPs is due to transcriptional activation of GRP94 and GRP78 genes, resulting in a rapid increase in the steady-state levels of GRP transcripts. From analysis of 5'-deletion mutants, the region of beta-mercaptoethanol responsiveness in the GRP78 promoter was mapped within 450 nucleotides upstream of the TATA sequence. This same general region was demonstrated to be important for induction of the GRP78 gene by the cal

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4

Kim, Y. K., and A. S. Lee. "Transcriptional activation of the glucose-regulated protein genes and their heterologous fusion genes by beta-mercaptoethanol." Molecular and Cellular Biology 7, no. 8 (1987): 2974–76. http://dx.doi.org/10.1128/mcb.7.8.2974.

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The sulfhydryl-reducing agent beta-mercaptoethanol preferentially stimulates the synthesis of glucose-regulated proteins (GRPs) in mammalian cells. The rapid and large increase in GRPs is due to transcriptional activation of GRP94 and GRP78 genes, resulting in a rapid increase in the steady-state levels of GRP transcripts. From analysis of 5'-deletion mutants, the region of beta-mercaptoethanol responsiveness in the GRP78 promoter was mapped within 450 nucleotides upstream of the TATA sequence. This same general region was demonstrated to be important for induction of the GRP78 gene by the cal

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5

Bitencourt, João Vitor Trindade, Paula Angélica Roratto, Marlise Ladvocat Bartholomei-Santos, and Sandro Santos. "Comparison of different methodologies for DNA extraction from Aegla longirostri." Brazilian Archives of Biology and Technology 50, no. 6 (2007): 989–94. http://dx.doi.org/10.1590/s1516-89132007000700010.

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The aim of this study was to compare some DNA extraction methodologies for Aegla longirostri. The protocols were based on the traditional phenol-chloroform DNA extraction methodology and using a commercial kit for DNA extraction. They differed in tissues used, the addition - or not - of beta-mercaptoethanol to the lysis buffer, times and methods for the animal's conservation (frozen, in ethanol or fresh). Individuals stored at -20°C for a long time supplied lower molecular weight DNA than those stored for a short time. The best yield for the specimens preserved in ethanol was obtained for 15 d

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6

Schnetkamp, P. P., R. T. Szerencsei, J. E. Tucker, and P. Van den Elzen. "Inhibition and acceleration of Na+/Ca2+/K+ exchange fluxes by Ag+ in bovine retinal rod outer segments." American Journal of Physiology-Cell Physiology 269, no. 5 (1995): C1147—C1152. http://dx.doi.org/10.1152/ajpcell.1995.269.5.c1147.

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The effect of Ag+ on Ca2+ fluxes mediated by the retinal rod Na+/Ca2+/K+ exchanger was investigated in intact bovine rod outer segments (ROS). Intracellular Na+ concentration ([Na+]in)-dependent Ca2+ influx and extracellular Na+ concentration ([Na+]out)-dependent Ca2+ efflux were monitored by changes in cytosolic free Ca2+ measured with the fluorescent Ca(2+)-indicating dye fluo 3. Ag+ was the most effective inhibitor of Na+/Ca2+/K+ exchange fluxes described to date, with half-maximal inhibition observed at 2-8 microM Ag+. Inhibition by Ag+ could be reversed by addition of beta-mercaptoethanol

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7

Chow, D. C., C. M. Browning, and J. G. Forte. "Gastric H(+)-K(+)-ATPase activity is inhibited by reduction of disulfide bonds in beta-subunit." American Journal of Physiology-Cell Physiology 263, no. 1 (1992): C39—C46. http://dx.doi.org/10.1152/ajpcell.1992.263.1.c39.

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H(+)-K(+)-ATPase activity of rabbit isolated gastric microsomes was irreversibly inactivated by reducing agents, such as 2-mercaptoethanol and dithiothreitol. Similar to what has been observed for Na(+)-K(+)-ATPase, high concentrations of reagents, at moderately elevated temperatures, were required to inactivate H(+)-K(+)-ATPase, suggesting relative inaccessibility of the responsible disulfide bonds. Resistance against inactivation was conferred by monovalent cation activators of K(+)-stimulated ATPase and p-nitro-phenylphosphatase. The effectiveness of K+ congeners in protecting the enzyme wa

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8

INUI, K. "EFFECTS OF BETA MERCAPTOETHANOL ON THE PROLIFERATION AND DIFFERENTIATION OF HUMAN OSTEOPROGENITOR CELLS." Cell Biology International 21, no. 7 (1997): 419–25. http://dx.doi.org/10.1006/cbir.1997.0165.

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9

Patchett, M. L., R. M. Daniel та H. W. Morgan. "Purification and properties of a stable β-glucosidase from an extremely thermophilic anaerobic bacterium". Biochemical Journal 243, № 3 (1987): 779–87. http://dx.doi.org/10.1042/bj2430779.

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A beta-glucosidase (EC 3.2.1.21) was purified to homogeneity from cell-free extracts of an extremely thermophilic anaerobic bacterium. The enzyme has an Mr of 43,000 as determined by molecular-exclusion chromatography, has a pI of 4.55 and shows optimum activity at pH 6.2. The enzyme is active against a wide range of aryl beta-glycosides and beta-linked disaccharides, with beta-galactosidase activity only slightly less than beta-glucosidase activity, and significant beta-xylosidase activity. Lineweaver-Burk plots for p-nitrophenyl beta-glucoside, o-nitrophenyl beta-glucoside and cellobiose sub

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10

Bailly, V., B. Sente та W. G. Verly. "Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but β-elimination and sometimes βδ-elimination catalysts". Biochemical Journal 259, № 3 (1989): 751–59. http://dx.doi.org/10.1042/bj2590751.

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Bacteriophage-T4 UV endonuclease nicks the C(3′)-O-P bond 3′ to AP (apurinic or apyrimidinic) sites by a beta-elimination reaction. The breakage of this bond is sometimes followed by the nicking of the C(5′)-O-P bond 5′ to the AP site, leaving a 3′-phosphate end; delta-elimination is proposed as a mechanism to explain this second reaction. The AP site formed when this enzyme acts on a pyrimidine dimer in a polynucleotide chain undergoes the same nicking reactions. Micrococcus luteus UV endonuclease also nicks the C(3′)-O-P bond 3′ to AP sites by a beta-elimination reaction. No subsequent delta

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